ID CRYL1_BOVIN Reviewed; 321 AA.
AC Q8SPX7;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 24-JAN-2024, entry version 115.
DE RecName: Full=Lambda-crystallin homolog;
DE EC=1.1.1.45 {ECO:0000250|UniProtKB:Q9Y2S2};
DE AltName: Full=L-gulonate 3-dehydrogenase;
DE Short=Gul3DH;
GN Name=CRYL1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12527201; DOI=10.1016/s0378-1119(02)01095-8;
RA Chen J., Yu L., Li D., Gao Q., Wang J., Huang X., Bi G., Wu H., Zhao S.;
RT "Human CRYL1, a novel enzyme-crystallin overexpressed in liver and kidney
RT and downregulated in 58% of liver cancer tissues from 60 Chinese patients,
RT and four new homologs from other mammalians.";
RL Gene 302:103-113(2003).
CC -!- FUNCTION: Has high L-gulonate 3-dehydrogenase activity. It also
CC exhibits low dehydrogenase activity toward L-3-hydroxybutyrate (HBA)
CC and L-threonate. {ECO:0000250|UniProtKB:Q9Y2S2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-gulonate + NAD(+) = 3-dehydro-L-gulonate + H(+) + NADH;
CC Xref=Rhea:RHEA:12889, ChEBI:CHEBI:13115, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57655, ChEBI:CHEBI:57945; EC=1.1.1.45;
CC Evidence={ECO:0000250|UniProtKB:Q9Y2S2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12890;
CC Evidence={ECO:0000250|UniProtKB:Q9Y2S2};
CC -!- ACTIVITY REGULATION: Inhibited by malonate.
CC {ECO:0000250|UniProtKB:Q9Y2S2}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9Y2S2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P14755}.
CC -!- SIMILARITY: Belongs to the 3-hydroxyacyl-CoA dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AF480862; AAL88550.1; -; mRNA.
DR RefSeq; NP_776718.1; NM_174293.2.
DR AlphaFoldDB; Q8SPX7; -.
DR SMR; Q8SPX7; -.
DR STRING; 9913.ENSBTAP00000066198; -.
DR PaxDb; 9913-ENSBTAP00000015575; -.
DR Ensembl; ENSBTAT00000015575.6; ENSBTAP00000015575.5; ENSBTAG00000011726.6.
DR GeneID; 281725; -.
DR KEGG; bta:281725; -.
DR CTD; 51084; -.
DR VEuPathDB; HostDB:ENSBTAG00000011726; -.
DR VGNC; VGNC:27744; CRYL1.
DR eggNOG; KOG2305; Eukaryota.
DR GeneTree; ENSGT00390000007182; -.
DR HOGENOM; CLU_009834_0_0_1; -.
DR InParanoid; Q8SPX7; -.
DR OMA; RDNCLTH; -.
DR OrthoDB; 5402028at2759; -.
DR TreeFam; TF313501; -.
DR Reactome; R-BTA-5661270; Formation of xylulose-5-phosphate.
DR Proteomes; UP000009136; Chromosome 12.
DR Bgee; ENSBTAG00000011726; Expressed in rumen papilla and 104 other cell types or tissues.
DR ExpressionAtlas; Q8SPX7; baseline and differential.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0050104; F:L-gulonate 3-dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0070403; F:NAD+ binding; ISS:UniProtKB.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR022694; 3-OHacyl-CoA_DH.
DR InterPro; IPR006180; 3-OHacyl-CoA_DH_CS.
DR InterPro; IPR006176; 3-OHacyl-CoA_DH_NAD-bd.
DR InterPro; IPR006108; 3HC_DH_C.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR48075; 3-HYDROXYACYL-COA DEHYDROGENASE FAMILY PROTEIN; 1.
DR PANTHER; PTHR48075:SF1; LAMBDA-CRYSTALLIN HOMOLOG; 1.
DR Pfam; PF00725; 3HCDH; 1.
DR Pfam; PF02737; 3HCDH_N; 1.
DR PIRSF; PIRSF000105; HCDH; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00067; 3HCDH; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; NAD; Oxidoreductase; Phosphoprotein; Reference proteome.
FT CHAIN 1..321
FT /note="Lambda-crystallin homolog"
FT /id="PRO_0000232505"
FT BINDING 19..20
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 39
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 100
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 105
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q811X6"
SQ SEQUENCE 321 AA; 35072 MW; 0BA232C7130F028C CRC64;
MASPGSSAPG GVAVVGSGLI GRSWAMLFAS AGFRVKLFDI EPRQVTDALV SLRKEMKMLE
LSGYLKGELG AEEQLSLISG CSDLREAVEG ALHVQECVPE NLELKRKLFA QLDKIADDHV
ILSSSSSCLL PSKLFAGLAH VKQCLVAHPV NPPYYVPLVE LVPHPETAPA TVDRTYALMR
RVGQSPVRLL REIDGFALNR LQYAVIAEAW RLVEEGVVSP GDLDLVMSDG LGLRYAFIGP
LETMHLNAEG MLSYCDRYGE GMKRVLKTFG PVPEFSGATA EKVHQAMCVK VPDDAEHLAA
RRAWRDGCLM RLAQLKHQLP Q
//
